Colicin E1 Binding to Membranes: Time-Resolved Studies of Spin-Labeled Mutants
| Autor: | Yeon-Kyun Shin, Françoise Levinthal, Wayne L. Hubbell, Cyrus Levinthal |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Lipid Bilayers
Mutant Colicins Protein Structure Secondary Adsorption Cysteine chemistry.chemical_classification Binding Sites Multidisciplinary Chemistry Cell Membrane Electron Spin Resonance Spectroscopy Wild type Hydrogen-Ion Concentration Peptide Fragments Kinetics Membrane Biochemistry Mutagenesis Colicin Thiol Biophysics Spin Labels Spin labeled |
| Zdroj: | Science. 259:960-963 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.8382373 |
| Popis: | To investigate the mechanism of interaction of the toxin colicin E1 with membranes, three cysteine substitution mutants and the wild type of the channel-forming fragment were spin labeled at the unique thiol. Time-resolved interaction of these labeled proteins with phospholipid vesicles was investigated with stopped-flow electron paramagnetic resonance spectroscopy. The fragment interacts with neutral bilayers at low pH, indicating that the interaction is hydrophobic rather than electrostatic. The interaction occurs in at least two distinct steps: (i) rapid adsorption to the surface; and (ii) slow, rate-limiting insertion of the hydrophobic central helices into the membrane interior. |
| Databáze: | OpenAIRE |
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